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Proteomic profile, biological activities and antigenic analysis of the venom from Bothriopsis bilineata smaragdina ("loro machaco"), a pitviper snake from Peru.
J Proteomics. 2018 09 15; 187:171-181.JP

Abstract

In order to determine Bothriopsis bilineata smaragdina venom (BbsV) composition, proteomic approaches were performed. Venom components were analyzed by RP-HPLC, SDS- PAGE and nano LC on line with LTQ Orbitrap XL. Results showed a total of 189 identified proteins, grouped into 11 different subgroups, which include snake venom metalloproteinases (SVMPs, 54.67%), snake C-type lectins (Snaclecs, 15.78%), snake venom serine proteinases (SVSPs, 14.69%), cystein-rich secretory proteins (CRISP, 2.61%), phospholipases A2 (PLA2, 1.14%), phosphodiesterase (PDE, 1.17%), venom endothelial growth factor (VEGF, 1.06%) 5'nucleotidases (0.33%), L-amino acid oxidases (LAAOs, 0.28%) and other proteins. In vitro enzymatic activities (SVMP, SVSP, LAAO, Hyal and PLA2) of BbsV were also analyzed. BbsV showed high SVSP activity but low PLA2 activity, when compared to other Bothrops venoms. In vivo, BbsV induced hemorrhage and edema in mice and showed intraperitoneal median lethal dose (LD50) of 92.74 (± 0.15) μg/20 g of mice. Furthermore, BbsV reduced cell viability when incubated with VERO cells. Peruvian and Brazilian bothropic antivenoms recognize BbsV proteins, as detected by ELISA and Western Blotting. Both antivenoms were able to neutralize in vivo edema and hemorrhage.

SIGNIFICANCE

In Peru, snakebite is a public health problem, especially in the rain forest, as a result of progressive colonization of this geographical area. This country is the second in Latin America, after Brazil, to exhibit the largest variety of venomous snakes. B. atrox and B. b. smaragdina snakes are sympatric species in Peruvian Amazon region and are responsible for approximately 95% of the envenomings reported in this region. B. b. smaragdina may cause a smaller share (3 to 38%) of those accidents, due to its arboreal habits, that make human encounters with these snakes less likely to happen. Despite B. b. smaragdina recognized medical importance, its venom composition and biological activities have been poorly studied. Furthermore, BbsV is not a component of the antigenic pool used to produce the corresponding Peruvian bothropic antivenom (P-BAV). Our results not only provide new insights on BbsV composition and biological activity, but also demonstrate that both P-BAV and B-BAV polyvalent antivenoms have a considerable recognition of proteins from BbsV and, more importantly, neutralized hemorrhage and edema, the main local effects of bothropic envenomation.

Authors+Show Affiliations

Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, 31270-901, Belo Horizonte, Minas Gerais, Brasil.Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, 21040-360, Rio de Janeiro, Brazil.Universidad Nacional Jorge Basadre Grohmann, Tacna, Perú.Centro de Pesquisa e Desenvolvimento, Fundação Ezequiel Dias, 30510-010, Belo Horizonte, MG, Brazil.Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, 31270-901, Belo Horizonte, Minas Gerais, Brasil.Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, 31270-901, Belo Horizonte, Minas Gerais, Brasil.Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, 31270-901, Belo Horizonte, Minas Gerais, Brasil.Faculdade de Medicina do Mucuri, Universidade Federal dos Vales do Jequitinhonha e Mucuri, 39803-371, Teófilo Otoni, Minas Gerais, Brasil.Universidad Nacional Mayor de San Marcos, Lima, Peru.Instituto Nacional de Salud, Lima, Peru.Centro de Pesquisa e Desenvolvimento, Fundação Ezequiel Dias, 30510-010, Belo Horizonte, MG, Brazil.Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, 21040-360, Rio de Janeiro, Brazil.Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, 31270-901, Belo Horizonte, Minas Gerais, Brasil. Electronic address: olortegi@icb.ufmg.br.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

30048773

Citation

Rodrigues, Carolina Rego, et al. "Proteomic Profile, Biological Activities and Antigenic Analysis of the Venom From Bothriopsis Bilineata Smaragdina ("loro Machaco"), a Pitviper Snake From Peru." Journal of Proteomics, vol. 187, 2018, pp. 171-181.
Rodrigues CR, Teixeira-Ferreira A, Vargas FFR, et al. Proteomic profile, biological activities and antigenic analysis of the venom from Bothriopsis bilineata smaragdina ("loro machaco"), a pitviper snake from Peru. J Proteomics. 2018;187:171-181.
Rodrigues, C. R., Teixeira-Ferreira, A., Vargas, F. F. R., Guerra-Duarte, C., Costal-Oliveira, F., Stransky, S., Lopes-de-Souza, L., Dutra, A. A. A., Yarlequé, A., Bonilla, C., Sanchez, E. F., Perales, J., & Chávez-Olórtegui, C. (2018). Proteomic profile, biological activities and antigenic analysis of the venom from Bothriopsis bilineata smaragdina ("loro machaco"), a pitviper snake from Peru. Journal of Proteomics, 187, 171-181. https://doi.org/10.1016/j.jprot.2018.07.016
Rodrigues CR, et al. Proteomic Profile, Biological Activities and Antigenic Analysis of the Venom From Bothriopsis Bilineata Smaragdina ("loro Machaco"), a Pitviper Snake From Peru. J Proteomics. 2018 09 15;187:171-181. PubMed PMID: 30048773.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Proteomic profile, biological activities and antigenic analysis of the venom from Bothriopsis bilineata smaragdina ("loro machaco"), a pitviper snake from Peru. AU - Rodrigues,Carolina Rego, AU - Teixeira-Ferreira,André, AU - Vargas,Frey Francisco Romero, AU - Guerra-Duarte,Clara, AU - Costal-Oliveira,Fernanda, AU - Stransky,Stephanie, AU - Lopes-de-Souza,Letícia, AU - Dutra,Alexandre Augusto Assis, AU - Yarlequé,Armando, AU - Bonilla,César, AU - Sanchez,Eladio Flores, AU - Perales,Jonas, AU - Chávez-Olórtegui,Carlos, Y1 - 2018/07/23/ PY - 2017/07/06/received PY - 2018/07/17/revised PY - 2018/07/21/accepted PY - 2018/7/27/pubmed PY - 2019/12/18/medline PY - 2018/7/27/entrez KW - Bothriopsis bilineata smaragdina KW - Peruvian snake KW - Venom characterization KW - Venom proteomics SP - 171 EP - 181 JF - Journal of proteomics JO - J Proteomics VL - 187 N2 - : In order to determine Bothriopsis bilineata smaragdina venom (BbsV) composition, proteomic approaches were performed. Venom components were analyzed by RP-HPLC, SDS- PAGE and nano LC on line with LTQ Orbitrap XL. Results showed a total of 189 identified proteins, grouped into 11 different subgroups, which include snake venom metalloproteinases (SVMPs, 54.67%), snake C-type lectins (Snaclecs, 15.78%), snake venom serine proteinases (SVSPs, 14.69%), cystein-rich secretory proteins (CRISP, 2.61%), phospholipases A2 (PLA2, 1.14%), phosphodiesterase (PDE, 1.17%), venom endothelial growth factor (VEGF, 1.06%) 5'nucleotidases (0.33%), L-amino acid oxidases (LAAOs, 0.28%) and other proteins. In vitro enzymatic activities (SVMP, SVSP, LAAO, Hyal and PLA2) of BbsV were also analyzed. BbsV showed high SVSP activity but low PLA2 activity, when compared to other Bothrops venoms. In vivo, BbsV induced hemorrhage and edema in mice and showed intraperitoneal median lethal dose (LD50) of 92.74 (± 0.15) μg/20 g of mice. Furthermore, BbsV reduced cell viability when incubated with VERO cells. Peruvian and Brazilian bothropic antivenoms recognize BbsV proteins, as detected by ELISA and Western Blotting. Both antivenoms were able to neutralize in vivo edema and hemorrhage. SIGNIFICANCE: In Peru, snakebite is a public health problem, especially in the rain forest, as a result of progressive colonization of this geographical area. This country is the second in Latin America, after Brazil, to exhibit the largest variety of venomous snakes. B. atrox and B. b. smaragdina snakes are sympatric species in Peruvian Amazon region and are responsible for approximately 95% of the envenomings reported in this region. B. b. smaragdina may cause a smaller share (3 to 38%) of those accidents, due to its arboreal habits, that make human encounters with these snakes less likely to happen. Despite B. b. smaragdina recognized medical importance, its venom composition and biological activities have been poorly studied. Furthermore, BbsV is not a component of the antigenic pool used to produce the corresponding Peruvian bothropic antivenom (P-BAV). Our results not only provide new insights on BbsV composition and biological activity, but also demonstrate that both P-BAV and B-BAV polyvalent antivenoms have a considerable recognition of proteins from BbsV and, more importantly, neutralized hemorrhage and edema, the main local effects of bothropic envenomation. SN - 1876-7737 UR - https://www.unboundmedicine.com/medline/citation/30048773/Proteomic_profile_biological_activities_and_antigenic_analysis_of_the_venom_from_Bothriopsis_bilineata_smaragdina__"loro_machaco"__a_pitviper_snake_from_Peru_ DB - PRIME DP - Unbound Medicine ER -